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Amino acid substitutions that stabilize the two-dimensional bacteriorhodopsin (BR) lattice, possibly by increasing increased lipid entropy, as has been suggested by Isenbarger and Krebs (2001). Two BR proteins of a BR trimer are shown, with the A–G helices of each indicated. The substitution of Ala for Ile at position 45 of the interface between the interacting B and D helices of neighbouring monomers is known to stabilize these complexes.
